Abstract
Bowman-Birk inhibitors (BBIs) are found primarily in seeds of legumes and in cereal grains. These canonical inhibitors share a highly conserved nine-amino acids binding loop motif CTP1SXPPXC (where P1 is the inhibitory active site, while X stands for various amino acids). They are natural controllers of plants’ endogenous proteases, but they are also inhibitors of exogenous proteases present in microbials and insects. They are considered as plants’ protective agents, as their elevated levels are observed during injury, presence of pathogens, or abiotic stress, i.a. Similar properties are observed for peptides isolated from amphibians’ skin containing 11-amino acids disulfide-bridged loop CWTP1SXPPXPC. They are classified as Bowman-Birk like trypsin inhibitors (BBLTIs). These inhibitors are resistant to proteolysis and not toxic, and they are reported to be beneficial in the treatment of various pathological states. In this review, we summarize up-to-date research results regarding BBIs’ and BBLTIs’ inhibitory activity, immunomodulatory and anti-inflammatory activity, antimicrobial and insecticidal strength, as well as chemopreventive properties.
Highlights
The complete set of proteases in an organism, known as a human degradome, is encoded by over 550 genes and represents more than 2% of the whole human genome [1]
Even though the classical soybean Birk inhibitors (BBIs) does not meet high initial expectations to become an effective, natural anticancer agent, it is shown that it might be considered as a complement for other molecules endowed with more evident anti-cancer properties, such as α-tocopheryl succinate or bioactive peptide lunasin
Various BBIs may be utilized as efficient tools for learning the exact role of proteolytic enzymes involved in diseases’ progress and development
Summary
The complete set of proteases in an organism, known as a human degradome, is encoded by over 550 genes and represents more than 2% of the whole human genome [1]. The BBIs family was established as a bunch of plant-derived inhibitors; a novel group of peptides originating from animals, which imitates the BBI’s trypsin inhibitory loop (TIL), has been recently identified [30,31,32]. These peptides were isolated from frogs’ skin, and to plant BBIs, they present strong trypsin inhibitory activity. Canonical inhibitors (standard mechanism inhibitors) include peptides and proteins grouped in at least 19 convergently evolved families [33] They are widely distributed in all forms of life and interact with target enzymes reversibly in a substrate-like manner [10,34]. A solution-state structural study revealed considerable flexibility in the protease binding loop and its conformational change upon binding to the enzyme [43]
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